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Using a Cyclic Ion Mobility Spectrometer for Tandem Ion Mobility Experiments
Published on: January 20, 2022
Structural separations by ion mobility-MS for glycomics and glycoproteomics
Larissa S Fenn1, John A McLean
1Department of Chemistry, Vanderbilt University, Nashville, TN, USA.
Methods in Molecular Biology (Clifton, N.J.)
|January 9, 2013
Summary
Ion mobility-mass spectrometry (IM-MS) offers powerful two-dimensional separations for detecting and characterizing glycoproteins and glycoconjugates. This technique distinguishes biomolecular classes and isomeric glycans, simplifying complex glycomic analyses.
Area of Science:
- Analytical Chemistry
- Biochemistry
- Glycoscience
Background:
- Glycoproteins and glycoconjugates play crucial roles in biological processes.
- Characterizing these complex molecules presents significant analytical challenges, particularly in distinguishing isomeric structures.
Purpose of the Study:
- To describe the utility of ion mobility-mass spectrometry (IM-MS) for glycoprotein and glycoconjugate analysis.
- To highlight IM-MS capabilities in separating complex glycan structures and associated peptides.
Main Methods:
- Ion mobility-mass spectrometry (IM-MS) provides separations based on both molecular structure/surface area and molecular mass.
- This dual-dimension separation allows for differentiation of various biomolecular classes and isobaric species.
Main Results:
- IM-MS enables the separation of peptides from associated glycans within the same sample digest without prior purification.
- The technique effectively separates different isomeric glycans, addressing a key challenge in current glycomic studies.
Conclusions:
- IM-MS is a valuable tool for the detection and characterization of glycoproteins and glycoconjugates.
- The methodologies detailed in this chapter facilitate the study of glycans and glycoproteins for both new and experienced practitioners.
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